Abstract:
:Tryptophan-rich antigens of malarial parasites interact with host molecules and play an important role in parasite survival. Merozoite expressed Plasmodium vivax tryptophan-rich antigen PvTRAg38 binds to human erythrocytes and facilitates parasite growth in a heterlologous Plasmodium falciparum culture system. Recently, we identified band 3 in human erythrocytes as one of its receptors, although the receptor-ligand binding mechanisms remain unknown. In the present study, using synthetic mutated peptides of PvTRAg38, we show that multiple amino acid residues of its 12 amino acid domain (KWVQWKNDKIRS) at position 197-208 interact with three different ectodomains of band 3 receptor on human erythrocytes. Our findings may help in the design of new therapeutic approaches for malaria.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Alam MS,Rathore S,Tyagi RK,Sharma YDdoi
10.1002/1873-3468.12053subject
Has Abstractpub_date
2016-01-01 00:00:00pages
232-41issue
2eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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